Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Christian Trncik"'
Publikováno v:
Nature Catalysis. 6:415-424
Autor:
Marta Vranas, Daniel Wohlwend, Danye Qiu, Stefan Gerhardt, Christian Trncik, Mehrosh Pervaiz, Kevin Ritter, Stefan Steimle, Antonio Randazzo, Oliver Einsle, Stefan Günther, Henning J. Jessen, Alexander Kotlyar, Thorsten Friedrich
Publikováno v:
Angewandte Chemie. 133:27483-27487
Autor:
Christian Trncik, Mehrosh Pervaiz, Thorsten Friedrich, Stefan Steimle, Stefan Gerhardt, Alexander Kotlyar, Danye Qiu, Stefan Günther, Antonio Randazzo, Henning J. Jessen, Marta Vranas, Kevin Ritter, Daniel Wohlwend, Oliver Einsle
Publikováno v:
Angewandte Chemie (International ed. in English). 60(52)
NADH:ubiquinone oxidoreductase, respiratory complex I, plays a central role in cellular energy metabolism. As a major source of reactive oxygen species (ROS) it affects ageing and mitochondrial dysfunction. The novel inhibitor NADH-OH specifically bl
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2353
Nitrogenases are the sole enzymes known to mediate biological nitrogen fixation, an essential process for sustaining life on earth. Among the three known variants, molybdenum nitrogenase is the best-studied to date. Recent work on the alternative van
Autor:
Michael Rohde, Katharina Grunau, Ivana Djurdjevic, Christian Trncik, Florian Schneider, Jakob Gies‐Elterlein, Oliver Einsle
Publikováno v:
Encyclopedia of Inorganic and Bioinorganic Chemistry. :1-10
Autor:
Dmitriy Lukoyanov, Lance C. Seefeldt, Neil L. Kelleher, Dennis R. Dean, Christian Trncik, Philip D. Compton, Oliver Einsle, Zhi-Yong Yang, Derek F. Harris, Hayden Kallas, Brian M. Hoffman
Publikováno v:
Biochemistry. 58:3293-3301
Three genetically distinct, but structurally similar, isozymes of nitrogenase catalyze biological N2 reduction to 2NH3: Mo-, V-, and Fe-nitrogenase, named respectively for the metal (M) in their ac...
Autor:
Casey Van Stappen, Justin T. Henthorn, Oliver Einsle, Joanna K. Kowalska, Christian Trncik, Serena DeBeer, David Keavney
Publikováno v:
Angewandte Chemie (International Ed. in English)
Nitrogenase enzymes catalyze the reduction of atmospheric dinitrogen to ammonia utilizing a Mo-7Fe-9S-C active site, the so-called FeMoco cluster. FeMoco and an analogous small-molecule (Et4 N)[(Tp)MoFe3 S4 Cl3 ] cubane have both been proposed to con
Publikováno v:
Methods in Molecular Biology ISBN: 9781071616048
Nitrogenases are the sole enzymes known to mediate biological nitrogen fixation, an essential process for sustaining life on earth. Among the three known variants, molybdenum nitrogenase is the best-studied to date. Recent work on the alternative van
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4b425cb485ce33030f2fe0e2be4a6f47
https://doi.org/10.1007/978-1-0716-1605-5_6
https://doi.org/10.1007/978-1-0716-1605-5_6
Publikováno v:
Journal of Inorganic Biochemistry. 227:111690
Biological nitrogen fixation, the conversion of atmospheric dinitrogen into bioavailable ammonium, is exclusively catalyzed by the enzyme nitrogenase that is present in nitrogen-fixing organisms, the diazotrophs. So far, three different nitrogenase v
Autor:
Ivana, Djurdjevic, Christian, Trncik, Michael, Rohde, Jakob, Gies, Katharina, Grunau, Florian, Schneider, Susana L A, Andrade, Oliver, Einsle
Publikováno v:
Metal ions in life sciences. 20
In biological nitrogen fixation, the enzyme nitrogenase mediates the reductive cleavage of the stable triple bond of gaseous N2at ambient conditions, driven by the hydrolysis of ATP, to yield bioavailable ammonium (NH4+). At the core of nitrogenase i